ID A0A2K6BNL6_MACNE Unreviewed; 245 AA.
AC A0A2K6BNL6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Eukaryotic translation initiation factor 6 {ECO:0000256|HAMAP-Rule:MF_03132};
DE Short=eIF-6 {ECO:0000256|HAMAP-Rule:MF_03132};
GN Name=EIF6 {ECO:0000256|HAMAP-Rule:MF_03132,
GN ECO:0000313|Ensembl:ENSMNEP00000012965.1};
GN Synonyms=ITGB4BP {ECO:0000256|HAMAP-Rule:MF_03132};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000012965.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000012965.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Binds to the 60S ribosomal subunit and prevents its
CC association with the 40S ribosomal subunit to form the 80S initiation
CC complex in the cytoplasm. Behaves as a stimulatory translation
CC initiation factor downstream insulin/growth factors. Is also involved
CC in ribosome biogenesis. Associates with pre-60S subunits in the nucleus
CC and is involved in its nuclear export. Cytoplasmic release of TIF6 from
CC 60S subunits and nuclear relocalization is promoted by a RACK1 (RACK1)-
CC dependent protein kinase C activity. In tissues responsive to insulin,
CC controls fatty acid synthesis and glycolysis by exerting translational
CC control of adipogenic transcription factors such as CEBPB, CEBPD and
CC ATF4 that have G/C rich or uORF in their 5'UTR. Required for ROS-
CC dependent megakaryocyte maturation and platelets formation, controls
CC the expression of mitochondrial respiratory chain genes involved in
CC reactive oxygen species (ROS) synthesis. Involved in miRNA-mediated
CC gene silencing by the RNA-induced silencing complex (RISC). Required
CC for both miRNA-mediated translational repression and miRNA-mediated
CC cleavage of complementary mRNAs by RISC. Modulates cell cycle
CC progression and global translation of pre-B cells, its activation seems
CC to be rate-limiting in tumorigenesis and tumor growth.
CC {ECO:0000256|HAMAP-Rule:MF_03132}.
CC -!- SUBUNIT: Monomer. Associates with the 60S ribosomal subunit. Interacts
CC with RACK1. Interacts with DICER1, AGO2, TARBP2, MOV10 and RPL7A; they
CC form a large RNA-induced silencing complex (RISC). {ECO:0000256|HAMAP-
CC Rule:MF_03132}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03132}.
CC Nucleus, nucleolus {ECO:0000256|HAMAP-Rule:MF_03132}. Note=Shuttles
CC between cytoplasm and nucleus/nucleolus. {ECO:0000256|HAMAP-
CC Rule:MF_03132}.
CC -!- PTM: Phosphorylation at Ser-174 and Ser-175 promotes nuclear export.
CC {ECO:0000256|HAMAP-Rule:MF_03132}.
CC -!- SIMILARITY: Belongs to the eIF-6 family. {ECO:0000256|HAMAP-
CC Rule:MF_03132}.
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DR RefSeq; XP_011764799.1; XM_011766497.1.
DR RefSeq; XP_011764800.1; XM_011766498.1.
DR AlphaFoldDB; A0A2K6BNL6; -.
DR SMR; A0A2K6BNL6; -.
DR STRING; 9545.ENSMNEP00000012965; -.
DR Ensembl; ENSMNET00000037164.1; ENSMNEP00000012965.1; ENSMNEG00000030745.1.
DR GeneID; 105496261; -.
DR KEGG; mni:105496261; -.
DR CTD; 3692; -.
DR GeneTree; ENSGT00390000015972; -.
DR OMA; LCHPKAT; -.
DR OrthoDB; 5473211at2759; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000030745; Expressed in adult mammalian kidney and 12 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005638; C:lamin filament; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0043023; F:ribosomal large subunit binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042256; P:cytosolic ribosome assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0035278; P:miRNA-mediated gene silencing by inhibition of translation; IEA:Ensembl.
DR GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl.
DR GO; GO:0042304; P:regulation of fatty acid biosynthetic process; IEA:Ensembl.
DR GO; GO:0006110; P:regulation of glycolytic process; IEA:Ensembl.
DR GO; GO:0045652; P:regulation of megakaryocyte differentiation; IEA:Ensembl.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IEA:Ensembl.
DR GO; GO:0032868; P:response to insulin; IEA:Ensembl.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IEA:UniProtKB-UniRule.
DR GO; GO:0000054; P:ribosomal subunit export from nucleus; IEA:UniProtKB-UniRule.
DR CDD; cd00527; IF6; 1.
DR HAMAP; MF_00032; eIF_6; 1.
DR InterPro; IPR002769; eIF6.
DR NCBIfam; TIGR00323; eIF-6; 1.
DR PANTHER; PTHR10784; EUKARYOTIC TRANSLATION INITIATION FACTOR 6; 1.
DR PANTHER; PTHR10784:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 6; 1.
DR Pfam; PF01912; eIF-6; 1.
DR PIRSF; PIRSF006413; IF-6; 1.
DR SMART; SM00654; eIF6; 1.
DR SUPFAM; SSF55909; Pentein; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03132};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW Rule:MF_03132}; Nucleus {ECO:0000256|HAMAP-Rule:MF_03132};
KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_03132};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_03132}; Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_03132}.
FT MOD_RES 165
FT /note="Phosphothreonine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03132"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03132"
FT MOD_RES 174
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03132"
FT MOD_RES 175
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03132"
SQ SEQUENCE 245 AA; 26599 MW; 5BA97CD5DB0C17C3 CRC64;
MAVRASFENN CEIGCFAKLT NTYCLVAIGG SENFYSVFEG ELSDTIPVVH ASIAGCRIIG
RMCVGNRHGL LVPNNTTDQE LQHIRNSLPD TVQIRRVEER LSALGNVTTC NDYVALVHPD
LDRETEEILA DVLKVEVFRQ TVADQVLVGS YCVFSNQGGL VHPKTSIEDQ DELSSLLQVP
LVAGTVNRGS EVIAAGMVVN DWCAFCGLDT TSTELSVVES VFKLNEAQPS TIATSMRDSL
IDSLT
//
